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- W1966692893 abstract "Amyloid-like aggregation of α-synuclein and deposit in Lewy bodies are thought to be the major cause of Parkinson′s disease. Here we describe the secondary structural transformation and aggregation of human α-synuclein and its C-terminus truncated fragments in trifluoroethanol. Proteins containing the NAC (non-amyloid component) segment undergo a three-state transition: from native random coil to β-sheet and to α-helical structure, while the NAC deficient fragment and γ-synuclein undergo a typical two-state coil-to-α transition. The β-sheet form is highly hydrophobic that strongly binds to 1-anilinonaphthalene-8-sulfonic acid (ANS) and is prone to self-aggregation. The results suggest that the NAC sequence is essential to β-sheet formation and the aggregation originates from the β-sheet intermediate, which may be implicated in the pathogenesis of Parkinson′s disease. © 2002 Wiley Periodicals, Inc. Biopolymers 64: 221–226, 2002" @default.
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- W1966692893 date "2002-06-03" @default.
- W1966692893 modified "2023-10-14" @default.
- W1966692893 title "Structural transformation and aggregation of human ?-synuclein in trifluoroethanol: Non-amyloid component sequence is essential and ?-sheet formation is prerequisite to aggregation" @default.
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- W1966692893 doi "https://doi.org/10.1002/bip.10179" @default.
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